PDCD2_HUMAN - dbPTM
PDCD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDCD2_HUMAN
UniProt AC Q16342
Protein Name Programmed cell death protein 2
Gene Name PDCD2
Organism Homo sapiens (Human).
Sequence Length 344
Subcellular Localization Nucleus .
Protein Description May be a DNA-binding protein with a regulatory function. May play an important role in cell death and/or in regulation of cell proliferation..
Protein Sequence MAAAGARPVELGFAESAPAWRLRSEQFPSKVGGRPAWLGAAGLPGPQALACELCGRPLSFLLQVYAPLPGRPDAFHRCIFLFCCREQPCCAGLRVFRNQLPRKNDFYSYEPPSENPPPETGESVCLQLKSGAHLCRVCGCLGPKTCSRCHKAYYCSKEHQTLDWRLGHKQACAQPDHLDHIIPDHNFLFPEFEIVIETEDEIMPEVVEKEDYSEIIGSMGEALEEELDSMAKHESREDKIFQKFKTQIALEPEQILRYGRGIAPIWISGENIPQEKDIPDCPCGAKRILEFQVMPQLLNYLKADRLGKSIDWGILAVFTCAESCSLGTGYTEEFVWKQDVTDTP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAAAGARPV
------CCCCCCCCC
13.15-
30UbiquitinationRSEQFPSKVGGRPAW
CHHHCCHHCCCCCCC
45.17-
30UbiquitinationRSEQFPSKVGGRPAW
CHHHCCHHCCCCCCC
45.17-
103UbiquitinationFRNQLPRKNDFYSYE
HHCCCCCCCCCCCCC
59.95-
103UbiquitinationFRNQLPRKNDFYSYE
HHCCCCCCCCCCCCC
59.95-
129UbiquitinationESVCLQLKSGAHLCR
CCEEHHCCCCCHHHH
33.60-
129UbiquitinationESVCLQLKSGAHLCR
CCEEHHCCCCCHHHH
33.60-
144UbiquitinationVCGCLGPKTCSRCHK
HCCCCCHHHHCCCCH
61.44-
144UbiquitinationVCGCLGPKTCSRCHK
HCCCCCHHHHCCCCH
61.44-
151UbiquitinationKTCSRCHKAYYCSKE
HHHCCCCHHHHCCCC
41.53-
157SumoylationHKAYYCSKEHQTLDW
CHHHHCCCCCCCCCC
56.51-
157UbiquitinationHKAYYCSKEHQTLDW
CHHHHCCCCCCCCCC
56.51-
157UbiquitinationHKAYYCSKEHQTLDW
CHHHHCCCCCCCCCC
56.51-
157SumoylationHKAYYCSKEHQTLDW
CHHHHCCCCCCCCCC
56.51-
239SumoylationKHESREDKIFQKFKT
HCCCHHHHHHHHHHH
40.44-
239UbiquitinationKHESREDKIFQKFKT
HCCCHHHHHHHHHHH
40.44-
239SumoylationKHESREDKIFQKFKT
HCCCHHHHHHHHHHH
40.44-
243UbiquitinationREDKIFQKFKTQIAL
HHHHHHHHHHHHHCC
37.77-
245UbiquitinationDKIFQKFKTQIALEP
HHHHHHHHHHHCCCH
46.70-
276UbiquitinationGENIPQEKDIPDCPC
CCCCCCCCCCCCCCC
56.56-
286UbiquitinationPDCPCGAKRILEFQV
CCCCCCCHHHHHHCH
25.84-
300PhosphorylationVMPQLLNYLKADRLG
HHHHHHHHHHHHHCC
15.0022817900
302UbiquitinationPQLLNYLKADRLGKS
HHHHHHHHHHHCCCC
37.57-
341PhosphorylationFVWKQDVTDTP----
EEEEECCCCCC----
42.3126074081
343PhosphorylationWKQDVTDTP------
EEECCCCCC------
22.8726074081

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDCD2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PDCD2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HCFC1_HUMANHCFC1physical
12149646
NCOR1_HUMANNCOR1physical
12149646
PRKN_HUMANPARK2physical
19146857

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PDCD2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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